[PDF][PDF] Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control

R Loewith, E Jacinto, S Wullschleger, A Lorberg… - Molecular cell, 2002 - cell.com
R Loewith, E Jacinto, S Wullschleger, A Lorberg, JL Crespo, D Bonenfant, W Oppliger…
Molecular cell, 2002cell.com
The target of rapamycin (TOR) proteins in Saccharomyces cerevisiae, TOR1 and TOR2,
redundantly regulate growth in a rapamycin-sensitive manner. TOR2 additionally regulates
polarization of the actin cytoskeleton in a rapamycin-insensitive manner. We describe two
functionally distinct TOR complexes. TOR Complex 1 (TORC1) contains TOR1 or TOR2,
KOG1 (YHR186c), and LST8. TORC2 contains TOR2, AVO1 (YOL078w), AVO2 (YMR068w),
AVO3 (YER093c), and LST8. FKBP-rapamycin binds TORC1, and TORC1 disruption mimics …
Abstract
The target of rapamycin (TOR) proteins in Saccharomyces cerevisiae, TOR1 and TOR2, redundantly regulate growth in a rapamycin-sensitive manner. TOR2 additionally regulates polarization of the actin cytoskeleton in a rapamycin-insensitive manner. We describe two functionally distinct TOR complexes. TOR Complex 1 (TORC1) contains TOR1 or TOR2, KOG1 (YHR186c), and LST8. TORC2 contains TOR2, AVO1 (YOL078w), AVO2 (YMR068w), AVO3 (YER093c), and LST8. FKBP-rapamycin binds TORC1, and TORC1 disruption mimics rapamycin treatment, suggesting that TORC1 mediates the rapamycin-sensitive, TOR-shared pathway. FKBP-rapamycin fails to bind TORC2, and TORC2 disruption causes an actin defect, suggesting that TORC2 mediates the rapamycin-insensitive, TOR2-unique pathway. Thus, the distinct TOR complexes account for the diversity, specificity, and selective rapamycin inhibition of TOR signaling. TORC1 and possibly TORC2 are conserved from yeast to man.
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